CLFB_STAAR
ID CLFB_STAAR Reviewed; 873 AA.
AC Q6GDH2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Clumping factor B;
DE AltName: Full=Fibrinogen receptor B;
DE AltName: Full=Fibrinogen-binding protein B;
DE Flags: Precursor;
GN Name=clfB; OrderedLocusNames=SAR2709;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Cell surface-associated protein implicated in virulence by
CC promoting bacterial attachment to both alpha- and beta-chains of human
CC fibrinogen and inducing the formation of bacterial clumps.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By
CC similarity). {ECO:0000250|UniProtKB:Q2FUY2}.
CC -!- DOMAIN: The Asp/Ser-rich domain functions as a stalk to allow the
CC ligand binding domain to be displayed in a functional form on the cell
CC surface. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads
CC to the inactivation of ClfB (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; BX571856; CAG41687.1; -; Genomic_DNA.
DR RefSeq; WP_000745917.1; NC_002952.2.
DR PDB; 4F1Z; X-ray; 2.30 A; A=197-542.
DR PDB; 4F20; X-ray; 2.50 A; A=197-542.
DR PDB; 4F24; X-ray; 2.51 A; A=197-542.
DR PDB; 4F27; X-ray; 1.92 A; A=197-542.
DR PDBsum; 4F1Z; -.
DR PDBsum; 4F20; -.
DR PDBsum; 4F24; -.
DR PDBsum; 4F27; -.
DR AlphaFoldDB; Q6GDH2; -.
DR SMR; Q6GDH2; -.
DR KEGG; sar:SAR2709; -.
DR HOGENOM; CLU_004137_1_2_9; -.
DR OMA; KPVHPSI; -.
DR OrthoDB; 243772at2; -.
DR PRO; PR:Q6GDH2; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000250"
FT CHAIN 45..837
FT /note="Clumping factor B"
FT /id="PRO_0000042012"
FT PROPEP 838..873
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000042013"
FT REGION 44..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..542
FT /note="Ligand binding A region"
FT /evidence="ECO:0000250"
FT REGION 530..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..26
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:Q2FUY2"
FT MOTIF 272..276
FT /note="MIDAS-like motif"
FT MOTIF 834..838
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 558..794
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 197..198
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
FT SITE 199..200
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
FT MOD_RES 837
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:4F24"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:4F27"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 317..329
FT /evidence="ECO:0007829|PDB:4F27"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 403..415
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:4F27"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:4F27"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4F27"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 485..493
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:4F27"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 518..529
FT /evidence="ECO:0007829|PDB:4F27"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:4F27"
SQ SEQUENCE 873 AA; 92996 MW; FC2093B51A4E71EF CRC64;
MKKRIDYLSN KQNKYSIRRF TVGTTSVIVG ATILFGIGNH QAQASEQSND TTQSSKNNAS
ADSEKNNTIE TPQLNTTAND TSDISANTNS ANVDSTAKTM STQTSNTTTT EPASTNETPQ
PTAIKDQATA AKMQDQTVPQ EANSQVDNKT TNDANNIATN SELKNPQTLD LPQSSPQTIS
NAQGTSKPSV RTRAVRSLAV AEPVVNAADA KGTNVNDKVT ASDFKLEKTA FDPNQSGNTF
MAANFKVTGQ VKSGDYFTAK LPDSVTGNGD VDYSNSNNTM PIADIKSTNG DVVAKATYDI
LTKTYTFVFT DYVNDKENIN GQFSLPLFTD RAKAPKSGTY DANINIADEM FDNKITYNYS
SPIAGIDKPN GANISSQIIG VDTASGQNTY KQTVFVNPKQ RVLGNTWVYI KGYQDKIEES
SGKVSATDTK LRIFEVNDTS KLSDSYYADP NDSNLKEVTG EFKDKISYKY DNVASINFGD
INKTYVVLVE GHYDNTGKNL KTQVIQENID PATGKDYSIF GWNNENVVRY GGGSADGDSA
VNPVDPTPGP PVDPEPEPEP TPDPEPSPEP EPEPTPDPEP SPEPDPDSDS DSDSGSDSDS
GSDSDSDSDS DSDSDSDSNS DSESDSDSDS DSDSDSDSDS DSDSDSDSDS DSESDSDSDS
DSDSDSDSDS DSDSDSDSNS DSDSDSDSDS DSDSDSDSDS DSESDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSES DSESDSDSDS ESDSDSDPDS ESDSDSDSDS DSDSDSDSES
DSDSESDSDS DSDSDSDSDS RVTPPNNEQK APSNPKGEVN HSNKASKQHQ TDALPETGDK
SENTNATLFD AMVALLGSLL LFRKRKQDHK EKA
